Structure of PDB 8jmo Chain B

Receptor sequence
>8jmoB (length=259) Species: 2725 (unidentified prokaryotic organism) [Search protein sequence]
MSNPYQRGPNPTRSALTADGPFSVATYTVSRLSVSGFGGGVIYYPTGTSL
TFGGIAMSPGYTADASSLAWLGRRLASHGFVVLVINTNSRFDGPDSRASQ
LSAALNYLRTSSPSAVRARLDANRLAVAGHAMGGGGTLRIAEQNPSLKAA
VPLTPWHTDKTFNTSVPVLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVY
VELCNASHIAPNSNNAAISVYTISWMKLWVDNDTRYRQFLCNVNDPALCD
FRTNNRHCQ
3D structure
PDB8jmo Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme.
ChainB
Resolution1.95 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.1.101: poly(ethylene terephthalate) hydrolase.
3.1.1.74: cutinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 E7J B G94 Y95 A165 M166 W190 V212 H242 G60 Y61 A131 M132 W156 V178 H208
Gene Ontology
Molecular Function
GO:0008126 acetylesterase activity
GO:0016787 hydrolase activity
GO:0050525 cutinase activity
GO:0052689 carboxylic ester hydrolase activity
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:8jmo, PDBe:8jmo, PDBj:8jmo
PDBsum8jmo
PubMed37979420
UniProtG9BY57|PETH_UNKP Leaf-branch compost cutinase

[Back to BioLiP]